Download citation
Download citation
link to html
A simple method for the preparation of isomorphous xenon derivatives is presented. A device has been designed that allows diffraction studies on protein crystals under xenon gas pressures up to 50 × 105 Pa. Crystal mounting and X-ray data collection do not significantly differ from standard techniques. Tests carried out on crystals of the protein porcine pancreatic elastase reveal a single xenon binding site with high occupancy at a pressure of 8 × 105 Pa. Xenon binding to several other crystallized proteins has also been investigated and results indicate that the method is generally applicable. Time-resolved studies show that, at 297 K, xenon binding is essentially completed within a few minutes. At pressures above 106 Pa, successful data collection is hampered by X-ray absorption and by the formation of xenon hydrate. Absorption can be reduced by using short-wavelength radiation and by mounting crystals in small capillaries. To circumvent xenon hydrate formation, higher working temperatures and the use of cryoprotective mother liquors are advocated.
Follow J. Appl. Cryst.
Sign up for e-alerts
Follow J. Appl. Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds